1. Fungicidal and binding properties of three plant peptides
A J De Lucca, T J Jacks, W J Broekaert Mycopathologia. 1998;144(2):87-91. doi: 10.1023/A:1007018423603.
The fungicidal properties of plant seed peptides from Heuchera sanginea (Hs-AFP1), Raphanus sativus (EA-AFP2), and Impatiens balsamina (Ib-AMP3) were determined for the non-germinated and germinated conidia of Aspergillus flavus and Fusarium moniliforme. These peptides were weakly lethal for germinated but not for non-germinated conidia of A. flavus. Both non-germinated and germinated conidia of F. moniliforme were susceptible to these peptides. Overall, F. moniliforme was more susceptible than A. flavus to the peptides. The peptides bound strongly to chitin, mannan, galactocerebrosides, and sphingomyelin. Binding results varied for ergosterol, cholesterol, and beta1,3-glucan.
2. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein
R H Tailor, D P Acland, S Attenborough, B P Cammue, I J Evans, R W Osborn, J A Ray, S B Rees, W F Broekaert J Biol Chem. 1997 Sep 26;272(39):24480-7. doi: 10.1074/jbc.272.39.24480.
Four closely related peptides were isolated from seed of Impatiens balsamina and were shown to be inhibitory to the growth of a range of fungi and bacteria, while not being cytotoxic to cultured human cells. The peptides, designated Ib-AMP1, Ib-AMP2, Ib-AMP3, and Ib-AMP4, are 20 amino acids long and are the smallest plant-derived antimicrobial peptides isolated to date. The Ib-AMPs (I. balsamina antimicrobial peptides) are highly basic and contain four cysteine residues which form two intramolecular disulfide bonds. Searches of protein data bases have failed to identify any proteins with significant homology to the peptides described here. Characterization of isolated cDNAs reveals that all four peptides are encoded within a single transcript. The predicted Ib-AMP precursor protein consists of a prepeptide followed by 6 mature peptide domains, each flanked by propeptide domains ranging from 16 to 35 amino acids in length. Such a primary structure with repeated alternating basic mature peptide domains and acidic propeptide domains has, to date, not been reported in plants.
